ID TAF1D_HUMAN Reviewed; 278 AA. AC Q9H5J8; Q6I9Y6; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 161. DE RecName: Full=TATA box-binding protein-associated factor RNA polymerase I subunit D; DE AltName: Full=RNA polymerase I-specific TBP-associated factor 41 kDa; DE Short=TAFI41; DE AltName: Full=TATA box-binding protein-associated factor 1D; DE Short=TBP-associated factor 1D; DE AltName: Full=Transcription initiation factor SL1/TIF-IB subunit D; GN Name=TAF1D; Synonyms=JOSD3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION. RX PubMed=15520167; DOI=10.1158/0008-5472.can-04-2801; RA Wang L., Bhattacharyya N., Chelsea D.M., Escobar P.F., Banerjee S.; RT "A novel nuclear protein, MGC5306 interacts with DNA polymerase beta and RT has a potential role in cellular phenotype."; RL Cancer Res. 64:7673-7677(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cervix; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION OF THE SL1/TIF-IB COMPLEX. RX PubMed=15970593; DOI=10.1074/jbc.m501595200; RA Friedrich J.K., Panov K.I., Cabart P., Russell J., Zomerdijk J.C.B.M.; RT "TBP-TAF complex SL1 directs RNA polymerase I pre-initiation complex RT formation and stabilizes upstream binding factor at the rDNA promoter."; RL J. Biol. Chem. 280:29551-29558(2005). RN [6] RP FUNCTION, IDENTIFICATION IN THE SL1/TIF-IB COMPLEX, INTERACTION WITH UBTF, RP AND SUBCELLULAR LOCATION. RX PubMed=17318177; DOI=10.1038/sj.emboj.7601601; RA Gorski J.J., Pathak S., Panov K., Kasciukovic T., Panova T., Russell J., RA Zomerdijk J.C.B.M.; RT "A novel TBP-associated factor of SL1 functions in RNA polymerase I RT transcription."; RL EMBO J. 26:1560-1568(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-234, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). CC -!- FUNCTION: Component of the transcription factor SL1/TIF-IB complex, CC which is involved in the assembly of the PIC (preinitiation complex) CC during RNA polymerase I-dependent transcription. The rate of PIC CC formation probably is primarily dependent on the rate of association of CC SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in CC stabilization of nucleolar transcription factor 1/UBTF on rDNA. CC Formation of SL1/TIF-IB excludes the association of TBP with TFIID CC subunits. {ECO:0000269|PubMed:15970593, ECO:0000269|PubMed:17318177}. CC -!- SUBUNIT: Component of the transcription factor SL1/TIF-IB complex, CC composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. Interacts CC with UBTF. {ECO:0000269|PubMed:17318177}. CC -!- INTERACTION: CC Q9H5J8; Q8NHQ1: CEP70; NbExp=4; IntAct=EBI-716128, EBI-739624; CC Q9H5J8; Q02577: NHLH2; NbExp=3; IntAct=EBI-716128, EBI-5378683; CC Q9H5J8; P06746: POLB; NbExp=4; IntAct=EBI-716128, EBI-713836; CC Q9H5J8; Q9H5J8: TAF1D; NbExp=3; IntAct=EBI-716128, EBI-716128; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15520167, CC ECO:0000269|PubMed:17318177}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK027016; BAB15628.1; -; mRNA. DR EMBL; CR457369; CAG33650.1; -; mRNA. DR EMBL; BC001972; AAH01972.1; -; mRNA. DR CCDS; CCDS8293.1; -. DR RefSeq; NP_077021.1; NM_024116.3. DR AlphaFoldDB; Q9H5J8; -. DR BioGRID; 122548; 97. DR ComplexPortal; CPX-7978; RNA polymerase I selectivity factor 1 compex. DR IntAct; Q9H5J8; 51. DR MINT; Q9H5J8; -. DR STRING; 9606.ENSP00000410409; -. DR iPTMnet; Q9H5J8; -. DR PhosphoSitePlus; Q9H5J8; -. DR BioMuta; TAF1D; -. DR DMDM; 74733586; -. DR EPD; Q9H5J8; -. DR jPOST; Q9H5J8; -. DR MassIVE; Q9H5J8; -. DR MaxQB; Q9H5J8; -. DR PaxDb; 9606-ENSP00000410409; -. DR PeptideAtlas; Q9H5J8; -. DR ProteomicsDB; 80916; -. DR Pumba; Q9H5J8; -. DR Antibodypedia; 53987; 66 antibodies from 12 providers. DR DNASU; 79101; -. DR Ensembl; ENST00000323981.6; ENSP00000314971.2; ENSG00000166012.17. DR Ensembl; ENST00000448108.7; ENSP00000410409.2; ENSG00000166012.17. DR Ensembl; ENST00000526015.5; ENSP00000435087.1; ENSG00000166012.17. DR GeneID; 79101; -. DR KEGG; hsa:79101; -. DR MANE-Select; ENST00000448108.7; ENSP00000410409.2; NM_024116.4; NP_077021.1. DR UCSC; uc001ped.5; human. DR AGR; HGNC:28759; -. DR CTD; 79101; -. DR DisGeNET; 79101; -. DR GeneCards; TAF1D; -. DR HGNC; HGNC:28759; TAF1D. DR HPA; ENSG00000166012; Low tissue specificity. DR MIM; 612823; gene. DR neXtProt; NX_Q9H5J8; -. DR OpenTargets; ENSG00000166012; -. DR PharmGKB; PA164726421; -. DR VEuPathDB; HostDB:ENSG00000166012; -. DR eggNOG; ENOG502SQMW; Eukaryota. DR GeneTree; ENSGT00390000009061; -. DR InParanoid; Q9H5J8; -. DR OMA; PLCSLID; -. DR OrthoDB; 4338834at2759; -. DR PhylomeDB; Q9H5J8; -. DR TreeFam; TF335756; -. DR PathwayCommons; Q9H5J8; -. DR Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression. DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression. DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression. DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation. DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape. DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination. DR SignaLink; Q9H5J8; -. DR SIGNOR; Q9H5J8; -. DR BioGRID-ORCS; 79101; 365 hits in 1126 CRISPR screens. DR ChiTaRS; TAF1D; human. DR GenomeRNAi; 79101; -. DR Pharos; Q9H5J8; Tdark. DR PRO; PR:Q9H5J8; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9H5J8; Protein. DR Bgee; ENSG00000166012; Expressed in body of pancreas and 202 other cell types or tissues. DR ExpressionAtlas; Q9H5J8; baseline and differential. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0072686; C:mitotic spindle; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro. DR InterPro; IPR027976; TAF1D. DR PANTHER; PTHR14562; TATA BOX-BINDING PROTEIN ASSOCIATED FACTOR RNA POLYMERASE I SUBUNIT D; 1. DR PANTHER; PTHR14562:SF3; TATA BOX-BINDING PROTEIN-ASSOCIATED FACTOR RNA POLYMERASE I SUBUNIT D; 1. DR Pfam; PF15333; TAF1D; 1. DR Genevisible; Q9H5J8; HS. PE 1: Evidence at protein level; KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..278 FT /note="TATA box-binding protein-associated factor RNA FT polymerase I subunit D" FT /id="PRO_0000250717" FT REGION 20..71 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 88..116 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 20..36 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 88..102 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 138 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 234 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT CONFLICT 14 FT /note="S -> T (in Ref. 3; CAG33650)" FT /evidence="ECO:0000305" FT CONFLICT 97 FT /note="R -> G (in Ref. 3; CAG33650)" FT /evidence="ECO:0000305" FT CONFLICT 278 FT /note="M -> I (in Ref. 3; CAG33650)" FT /evidence="ECO:0000305" SQ SEQUENCE 278 AA; 32058 MW; 4BA37C73BB387446 CRC64; MDKSGIDSLD HVTSDAVELA NRSDNSSDSS LFKTQCIPYS PKGEKRNPIR KFVRTPESVH ASDSSSDSSF EPIPLTIKAI FERFKNRKKR YKKKKKRRYQ PTGRPRGRPE GRRNPIYSLI DKKKQFRSRG SGFPFLESEN EKNAPWRKIL TFEQAVARGF FNYIEKLKYE HHLKESLKQM NVGEDLENED FDSRRYKFLD DDGSISPIEE STAEDEDATH LEDNECDIKL AGDSFIVSSE FPVRLSVYLE EEDITEEAAL SKKRATKAKN TGQRGLKM //